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Protein

Cysteine desulfurase, mitochondrial

Gene

NFS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. Plays a role in both tRNA-processing and mitochondrial metabolism. Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.5 Publications

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.1 Publication

Cofactori

pyridoxal 5'-phosphateBy similarity

pH dependencei

Optimum pH is 8.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei248 – 2481Pyridoxal phosphateBy similarity
Binding sitei276 – 2761Pyridoxal phosphateBy similarity
Binding sitei336 – 3361Pyridoxal phosphateBy similarity
Active sitei421 – 4211Cysteine persulfide intermediateBy similarity
Metal bindingi421 – 4211Iron-sulfur (2Fe-2S); via persulfide groupBy similarity

GO - Molecular functioni

GO - Biological processi

  • [2Fe-2S] cluster assembly Source: InterPro
  • cellular iron ion homeostasis Source: SGD
  • iron-sulfur cluster assembly Source: SGD
  • mitochondrial tRNA thio-modification Source: SGD
  • tRNA thio-modification Source: SGD
  • tRNA wobble uridine modification Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29283-MONOMER.
YEAST:G3O-29283-MONOMER.
ReactomeiR-SCE-1362409. Mitochondrial iron-sulfur cluster biogenesis.
R-SCE-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.
R-SCE-947581. Molybdenum cofactor biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine desulfurase, mitochondrial1 Publication (EC:2.8.1.71 Publication)
Alternative name(s):
tRNA-splicing protein SPL11 Publication
Gene namesi
Name:NFS1Imported
Synonyms:SPL11 Publication
Ordered Locus Names:YCL017CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCL017C.
SGDiS000000522. NFS1.

Subcellular locationi

GO - Cellular componenti

  • L-cysteine desulfurase complex Source: SGD
  • mitochondrion Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Impairs cysteine desulfurase activity of mitochondria. Leads to strong accumulation of free iron, not bound to heme or Fe/S clusters, in mitochondria, as well as to decreased amounts of the mitochondrial Fe/S proteins including aconitase and succinate dehydrogenase. Leads also to accumulation of 5-methoxycarbonylmethyluridine (mcm5U) and a concomitant decrease in 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi191 – 1911I → S: Exhibits constitutive up-regulation of the genes of the cellular iron uptake system. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence analysisAdd
BLAST
Chaini34 – 497464Cysteine desulfurase, mitochondrialPRO_0000001304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiP25374.
PRIDEiP25374.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ISD11Q6Q56010EBI-11991,EBI-784315
ISU1Q030202EBI-11991,EBI-29901

Protein-protein interaction databases

BioGridi30967. 24 interactions.
DIPiDIP-2948N.
IntActiP25374. 14 interactions.
MINTiMINT-474525.

Structurei

3D structure databases

ProteinModelPortaliP25374.
SMRiP25374. Positions 99-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni168 – 1692Pyridoxal phosphate bindingBy similarity
Regioni296 – 2983Pyridoxal phosphate bindingBy similarity

Domaini

the N-terminal beta-strand formed by residues 99-104 is essential for the function.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063513.
HOGENOMiHOG000017510.
InParanoidiP25374.
KOiK04487.
OMAiDNMAIRG.
OrthoDBiEOG092C2OKO.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00331. Cys_desulf_IscS. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase_IscS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02006. IscS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKSTATRSI TRLSQVYNVP AATYRACLVS RRFYSPPAAG VKLDDNFSLE
60 70 80 90 100
THTDIQAAAK AQASARASAS GTTPDAVVAS GSTAMSHAYQ ENTGFGTRPI
110 120 130 140 150
YLDMQATTPT DPRVLDTMLK FYTGLYGNPH SNTHSYGWET NTAVENARAH
160 170 180 190 200
VAKMINADPK EIIFTSGATE SNNMVLKGVP RFYKKTKKHI ITTRTEHKCV
210 220 230 240 250
LEAARAMMKE GFEVTFLNVD DQGLIDLKEL EDAIRPDTCL VSVMAVNNEI
260 270 280 290 300
GVIQPIKEIG AICRKNKIYF HTDAAQAYGK IHIDVNEMNI DLLSISSHKI
310 320 330 340 350
YGPKGIGAIY VRRRPRVRLE PLLSGGGQER GLRSGTLAPP LVAGFGEAAR
360 370 380 390 400
LMKKEFDNDQ AHIKRLSDKL VKGLLSAEHT TLNGSPDHRY PGCVNVSFAY
410 420 430 440 450
VEGESLLMAL RDIALSSGSA CTSASLEPSY VLHALGKDDA LAHSSIRFGI
460 470 480 490
GRFSTEEEVD YVVKAVSDRV KFLRELSPLW EMVQEGIDLN SIKWSGH
Length:497
Mass (Da):54,467
Last modified:March 15, 2004 - v2
Checksum:iD709E326B3921BCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501H → Y in AAA34814 (PubMed:8444805).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98808 Genomic DNA. Translation: AAA34814.1.
X59720 Genomic DNA. Translation: CAA42344.2.
M12909 Genomic DNA. Translation: AAA66918.1.
BK006937 Genomic DNA. Translation: DAA07466.1.
PIRiS19343.
RefSeqiNP_009912.2. NM_001178664.1.

Genome annotation databases

EnsemblFungiiCAA42344; CAA42344; CAA42344.
YCL017C; YCL017C; YCL017C.
GeneIDi850343.
KEGGisce:YCL017C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98808 Genomic DNA. Translation: AAA34814.1.
X59720 Genomic DNA. Translation: CAA42344.2.
M12909 Genomic DNA. Translation: AAA66918.1.
BK006937 Genomic DNA. Translation: DAA07466.1.
PIRiS19343.
RefSeqiNP_009912.2. NM_001178664.1.

3D structure databases

ProteinModelPortaliP25374.
SMRiP25374. Positions 99-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30967. 24 interactions.
DIPiDIP-2948N.
IntActiP25374. 14 interactions.
MINTiMINT-474525.

Proteomic databases

MaxQBiP25374.
PRIDEiP25374.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42344; CAA42344; CAA42344.
YCL017C; YCL017C; YCL017C.
GeneIDi850343.
KEGGisce:YCL017C.

Organism-specific databases

EuPathDBiFungiDB:YCL017C.
SGDiS000000522. NFS1.

Phylogenomic databases

GeneTreeiENSGT00530000063513.
HOGENOMiHOG000017510.
InParanoidiP25374.
KOiK04487.
OMAiDNMAIRG.
OrthoDBiEOG092C2OKO.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29283-MONOMER.
YEAST:G3O-29283-MONOMER.
ReactomeiR-SCE-1362409. Mitochondrial iron-sulfur cluster biogenesis.
R-SCE-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.
R-SCE-947581. Molybdenum cofactor biosynthesis.

Miscellaneous databases

PROiP25374.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00331. Cys_desulf_IscS. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase_IscS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02006. IscS. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNFS1_YEAST
AccessioniPrimary (citable) accession number: P25374
Secondary accession number(s): D6VQZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 15, 2004
Last modified: September 7, 2016
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 504 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.